NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 6207 / DSM 20271 / IFO 12424 / LMG 16412 / NCTC 10470;
DOI=10.1007/s002530050945; PubMed=9163953 [NCBI, ExPASy, EBI, Israel, Japan]
Hashimoto Y., Yamashita Y., Murooka Y.;
"The Propionibacterium freudenreichii hemYHBXRL gene cluster, which encodes enzymes and a regulator involved in the biosynthetic pathway from glutamate to protoheme.";
Appl. Microbiol. Biotechnol. 47:385-392(1997).

Comments

FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
CATALYTIC ACTIVITY: Protoporphyrinogen-IX + 3 O₂ = protoporphyrin-IX + 3 H₂O₂.
COFACTOR: Binds 1 FAD per dimer (By similarity).
PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1 .
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the protoporphyrinogen oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D85417; BAA21909.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

O32434.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0004729;	Molecular function: protoporphyrinogen oxidase activity (inferred from electronic annotation from InterPro).
GO:0006783;	Biological process: heme biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002937; Amino_oxidase.
IPR016040; NAD(P)-bd.
IPR004572; Proto_IX_ox.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF01593; Amino_oxidase; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00562; proto_IX_ox; 1.

ProtoNet

O32434.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; FAD; Flavoprotein; Heme biosynthesis; Oxidoreductase; Porphyrin biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 527`	`527`	`Protoporphyrinogen oxidase.`	`PRO_0000135268`
`NP_BIND`	`33 38`	`6`	`FAD (Potential).`

Sequence information

Length: 527 AA [This is the length of the unprocessed precursor]

Molecular weight: 55268 Da [This is the MW of the unprocessed precursor]

CRC64: 579CB0A3318BF938 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTTDRVTTP TPTVSGTDAP GPDASHCHLV VVGGGITGLA AAWQGMARGA RVSVVESDDH 

        70         80         90        100        110        120 
FGGKVVTDRR DGFLVEQGPD SFVAYRPAAL KLIEELGLSD QVIAPGGGRR VSLLSRGKLR 

       130        140        150        160        170        180 
PMPAGMGMVL PTRMWPFVTT TVLSWPDKIR AGLDLVIPRR LPDHDVAIGA FLRQRLGDGI 

       190        200        210        220        230        240 
VRRFADPMVG GIYGAGIDEL SLDAVLPSLR DNERDHRSLM VASLAGGRAS RRAARQRAAQ 

       250        260        270        280        290        300 
NNAQQNSSHQ NSTGQNNSAG TRGPAASPFR TLRGGLGQLI DALVDQLRAG GVELLVNTSV 

       310        320        330        340        350        360 
DLLGRDGVHL SDGRVLPADA VVLAGGVASS ARLLRPQLPA AARALAQIPL ASTTIVSLAW 

       370        380        390        400        410        420 
PVSAFDVAPD SQGWLEADAG PVSGLTASSI KFAGRAPDGS VLMRVFVPDK RGPLTDAPDD 

       430        440        450        460        470        480 
ELLSAVIDHV RPLLGVHGEP GLTQITRWHK VMPKYTVGHL ERAAVVDSTL AEQRPTWAVA 

       490        500        510        520 
GSALHGVGLP DCISDARHSA DEVIDAALAA TPSAPNRNAA TDRTETR

O32434 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools